Positively and negatively charged residues have different effects on the position in the membrane of a model transmembrane helix

J Mol Biol. 1998 Dec 11;284(4):1177-83. doi: 10.1006/jmbi.1998.2218.

Abstract

We have studied the effects of single charged residues on the position of a model transmembrane helix in the endoplasmic reticulum membrane using the glycosylation mapping technique. Asp and Glu residues cause a re-positioning of the C-terminal end of the transmembrane helix when placed in the one to two C-terminal turns but not when placed more centrally. Arg and Lys residues, in contrast, have little effect when placed in the two C-terminal turn but give rise to a more substantial shift in position when placed 9-11 residues from the helix end. We suggest that this difference between the effects of positively and negatively charged residues can be explained by the so-called snorkel effect, i.e. that the very long side-chains of Arg and Lys can reach up along the transmembrane helix to allow the terminal, charged moiety to reside in the lipid headgroup region while the Calpha of the residue is positioned well below the membrane/water interface.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / chemistry
  • Bacteriophage M13 / chemistry
  • Bacteriophage M13 / genetics
  • Capsid / chemistry
  • Capsid / genetics
  • Capsid Proteins*
  • Electrochemistry
  • Glycosylation
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Peptides / chemistry
  • Protein Structure, Secondary

Substances

  • Amino Acids
  • Capsid Proteins
  • Membrane Proteins
  • Peptides
  • coat protein, Bacteriophage M13
  • polyleucine